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Lipase catalyzed transesterification of ethyl butyrate synthesis in n-hexane— a kinetic study

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Abstract

Kinetics of lipase catalyzed transesterification of ethyl caprate and butyric acid was investigated. The objective of this work was to propose a reaction mechanism and develop a rate equation for the synthesis of ethyl butyrate by transesterification using surfactant coated lipase from Candida rugosa. The reaction rate could be described in terms of Michaelis–Menten equation with a Ping-Pong Bi–Bi mechanism and competitive inhibition by both the substrates. The values of kinetic parameters computed were Vmax = 2.861 μmol/min/mg; Km(acid) = 0.0746 M; Km(ester) = 0.125 M; Ki acid = 0.450 M. This study indicated a competitive enzyme inhibition by butyric acid during lipase catalyzed transesterification reaction. Experimental observations had clearly indicated that the substrates as well as product act as dead-end inhibitors.

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Acknowledgements

The authors are thankful to the Principal, Dr. K.V.L. Raju and the management of MVGR College of Engineering, Vizianagaram, (A.P.) for their constant support and encouragement.

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Correspondence to N. Annapurna Devi.

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Devi, N.A., Radhika, G.B. & Bhargavi, R.J. Lipase catalyzed transesterification of ethyl butyrate synthesis in n-hexane— a kinetic study. J Food Sci Technol 54, 2871–2877 (2017). https://doi.org/10.1007/s13197-017-2725-2

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  • DOI: https://doi.org/10.1007/s13197-017-2725-2

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